Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography

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dc.contributor.author Bogema, DR
dc.contributor.author Deutscher, AT
dc.contributor.author Woolley, LK
dc.contributor.author Seymour, LM
dc.contributor.author Raymond, BBA
dc.contributor.author Tacchi, JL
dc.contributor.author Padula, MP
dc.contributor.author Dixon, NE
dc.contributor.author Minion, FC
dc.contributor.author Jenkins, C
dc.contributor.author Walker, MJ
dc.contributor.author Djordjevic, SP
dc.date.accessioned 2012-10-12T03:33:24Z
dc.date.issued 2012-03
dc.identifier.citation mBio, 2012, 3 (2)
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18117
dc.description.abstract Mycoplasma hyopneumoniae causes enormous economic losses to swine production worldwide by colonizing the ciliated epithelium in the porcine respiratory tract, resulting in widespread damage to the mucociliary escalator, prolonged inflammation, reduced weight gain, and secondary infections. Protein Mhp684 (P146) comprises 1,317 amino acids, and while the N-terminal 400 residues display significant sequence identity to the archetype cilium adhesin P97, the remainder of the molecule is novel and displays unusual motifs. Proteome analysis shows that P146 preprotein is endogenously cleaved into three major fragments identified here as P50P146, P40P146, and P85P146 that reside on the cell surface. Liquid chromatography with tandem mass spectrometry (LC-MS/MS) identified a semitryptic peptide that delineated a major cleavage site in Mhp684. Cleavage occurred at the phenylalanine residue within sequence 672ATEF↓QQ677, consistent with a cleavage motif resembling S/T-X-F↓XD/E recently identified in Mhp683 and other P97/P102 family members. Biotinylated surface proteins recovered by avidin chromatography and separated by two-dimensional gel electrophoresis (2-D GE) showed that more-extensive endoproteolytic cleavage of P146 occurs. Recombinant fragments F1P146-F3P146 that mimic P50P146, P40P146, and P85P146 were constructed and shown to bind porcine epithelial cilia and biotinylated heparin with physiologically relevant affinity. Recombinant versions of F3P146 generated from M. hyopneumoniae strain J and 232 sequences strongly bind porcine plasminogen, and the removal of their respective C-terminal lysine and arginine residues significantly reduces this interaction. These data reveal that P146 is an extensively processed, multifunctional adhesin of M. hyopneumoniae. Extensive cleavage coupled with variable cleavage efficiency provides a mechanism by which M. hyopneumoniae regulates protein topography. © 2012 Bogema et al.
dc.language eng
dc.relation.isbasedon 10.1128/mBio.00282-11
dc.title Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography
dc.type Journal Article
dc.description.version Published
dc.parent mBio
dc.journal.volume 2
dc.journal.volume 3
dc.journal.number 2 en_US
dc.publocation United States en_US
dc.identifier.startpage 1 en_US
dc.identifier.endpage en_US
dc.identifier.endpage 11 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 0605 Microbiology
dc.personcode 970082
dc.personcode 107126
dc.personcode 119529
dc.personcode 117836
dc.personcode 113696
dc.personcode 108199
dc.percentage 100 en_US
dc.classification.name Microbiology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - i3
pubs.organisational-group /University of Technology Sydney/Students
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true


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